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Nucleic Acids Research, 1988, Vol. 16, No. 6 2565-2585
© 1988

Articles

RNA binding proteins of the large subunit of bovine mitochondrial ribosomes

Mieczyslaw A. Piatyszek+, Nancy D. Denslow and W. O'Brien

Department of Biochemistry and Molecular Biology, University of Florida Gainesville, FL 32610, USA

Received October 20, 1987. Revised February 24, 1988. Accepted February 24, 1988.

RNA binding properties of proteins from the large subunit of bovine mitochondrial ribosomes were studied using four different approaches: binding of radiolabeled RNA to western blotted proteins; disassembly of the intact 39 S ribosomal subunits with urea; binding of ribosomal proteins to RNA in the presence of urea; and binding of proteins extracted with lithium chloride to RNA. Results from these four approaches allowed us to identify a set of six proteins (L7, L13, L14, L21, L26, and L44) which appear to be strong RNA binding proteins. Seven additional proteins (L8, L11, L28, L35, L40, L49, and L50) were identified as secondary RNA binding proteins. RNA binding properties of the proteins in both of these sets were compared with the topographic disposition and susceptibility towards lithium chloride extraction of the individual proteins. Proteins from the first set are good candidates for early assembly proteins since they have a high affinity for RNA, are generally found in 4M lithium chloride core particles, and are among the most buried proteins in the 39 S subunit.

+Present address: Department of Biopolymer Biochemistry, A. Mickiewicz University, Fredry 10, Poznan 61-701, Polond.


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